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Volumn 15, Issue PART A., 1996, Pages 161-192

Preparation Of Immobilized Proteins Covalently Coupled Through Silane Coupling Agents To Inorganic Supports

(1)  Weetall, Howard H a  

a NONE

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EID: 0005673235     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(08)60308-2     Document Type: Article
Times cited : (5)

References (104)
  • 1
    • 0025139135 scopus 로고
    • Direct liquid chromatographic separation of enantiomers on immobilized protein stationary phases VIII. A comparison of a series of sorbents based on bovine serum albumin and its fragments
    • Andersson S., Allenmark S., Erlandsson P., and Nilsson S. Direct liquid chromatographic separation of enantiomers on immobilized protein stationary phases VIII. A comparison of a series of sorbents based on bovine serum albumin and its fragments. J. Chromatogr. 498 (1990) 81
    • (1990) J. Chromatogr. , vol.498 , pp. 81
    • Andersson, S.1    Allenmark, S.2    Erlandsson, P.3    Nilsson, S.4
  • 2
    • 0024366874 scopus 로고
    • Isolation of a specific membrane protein by immunoaffinity chromatography with biotinylated antibodies immobilized on avidin coated glass beads
    • Babashak J.V., and Phillips T.M. Isolation of a specific membrane protein by immunoaffinity chromatography with biotinylated antibodies immobilized on avidin coated glass beads. J. Chromatogr. 476 (1988) 187
    • (1988) J. Chromatogr. , vol.476 , pp. 187
    • Babashak, J.V.1    Phillips, T.M.2
  • 3
    • 0023904324 scopus 로고
    • Use of Avidin-coated glass beads as a support for high-performance immunoaffinity chromatography
    • Babashak J.V., and Phillips T.M. Use of Avidin-coated glass beads as a support for high-performance immunoaffinity chromatography. J. Chromatogr. 444 (1988) 21
    • (1988) J. Chromatogr. , vol.444 , pp. 21
    • Babashak, J.V.1    Phillips, T.M.2
  • 5
    • 0024405138 scopus 로고
    • Improved resolution of glycoproteins by chromatography with concanavalin A immobilized on microparticulate silica via temperature-programmed elution
    • Bergold A.F., and Carr P.W. Improved resolution of glycoproteins by chromatography with concanavalin A immobilized on microparticulate silica via temperature-programmed elution. Anal. Chem. 61 (1989) 1117
    • (1989) Anal. Chem. , vol.61 , pp. 1117
    • Bergold, A.F.1    Carr, P.W.2
  • 6
    • 0026325893 scopus 로고
    • Immobilization of Fv antibody fragments on porous silica and their utility in affinity chromatography
    • Berry M.J., Davies J., Smith C.G., and Smith I. Immobilization of Fv antibody fragments on porous silica and their utility in affinity chromatography. J. Chromatogr. 587 (1991) 161
    • (1991) J. Chromatogr. , vol.587 , pp. 161
    • Berry, M.J.1    Davies, J.2    Smith, C.G.3    Smith, I.4
  • 9
    • 77956728380 scopus 로고
    • Epiamine coupling to inorganic supports
    • U.S. Patent No. 4, 415, 664
    • Bursecz, C.F. (1983). Epiamine coupling to inorganic supports. U.S. Patent No. 4, 415, 664.
    • (1983)
    • Bursecz, C.F.1
  • 10
    • 0021479449 scopus 로고
    • A simple kinetic model for the hydrolysis of alpha-D-glucans using glucoamylase EC-3.2.1.3 immobilized on titanium-IV activated porous silica
    • Cabral J.M.S., Cardoso J.P., Novias J.M., and Kennedy J.F. A simple kinetic model for the hydrolysis of alpha-D-glucans using glucoamylase EC-3.2.1.3 immobilized on titanium-IV activated porous silica. Enzyme Microb. Technol. 6 (1984) 365
    • (1984) Enzyme Microb. Technol. , vol.6 , pp. 365
    • Cabral, J.M.S.1    Cardoso, J.P.2    Novias, J.M.3    Kennedy, J.F.4
  • 11
    • 0024016187 scopus 로고
    • Preparation and activity of carbonic anhydrase immobilized on porous silica beads and graphite rods
    • Crumbliss A.L., McLachlan K.L., O'Daly J.P., and Henkens R.W. Preparation and activity of carbonic anhydrase immobilized on porous silica beads and graphite rods. Biotechnol. Bioeng. 31 (1988) 796
    • (1988) Biotechnol. Bioeng. , vol.31 , pp. 796
    • Crumbliss, A.L.1    McLachlan, K.L.2    O'Daly, J.P.3    Henkens, R.W.4
  • 12
    • 0021739234 scopus 로고
    • Compositional analysis of proteins following hydrolysis by immobilized proteases
    • Church F.C., Swaisgood H.E., and Catignani G.L. Compositional analysis of proteins following hydrolysis by immobilized proteases. J. Appl. Biochem. 6 (1984) 205
    • (1984) J. Appl. Biochem. , vol.6 , pp. 205
    • Church, F.C.1    Swaisgood, H.E.2    Catignani, G.L.3
  • 13
    • 0039056485 scopus 로고
    • Immobilized enzymes on semiconducting powder photogeneration of hydrogen by titanium dioxide and cadmium sulfide bound hydro-genases
    • Cuendet P., Gratzel M., Rao K.K., and Hall D.O. Immobilized enzymes on semiconducting powder photogeneration of hydrogen by titanium dioxide and cadmium sulfide bound hydro-genases. Photobiochem. Photobiophys. 7 (1984) 331
    • (1984) Photobiochem. Photobiophys. , vol.7 , pp. 331
    • Cuendet, P.1    Gratzel, M.2    Rao, K.K.3    Hall, D.O.4
  • 14
    • 0023130156 scopus 로고
    • Separation of blood group A-active oligosaccharides by high-pressure liquid affinity chromatography with concanavalin A immobilized by metal interactions on the stationary phase
    • Dakour J., Lundblad A., and Dopf D. Separation of blood group A-active oligosaccharides by high-pressure liquid affinity chromatography with concanavalin A immobilized by metal interactions on the stationary phase. Anal. Biochem. 161 (1988) 140
    • (1988) Anal. Biochem. , vol.161 , pp. 140
    • Dakour, J.1    Lundblad, A.2    Dopf, D.3
  • 15
    • 0025046786 scopus 로고
    • Application of magnetic immobilized beta-glucosidase in the enzymatic saccari-fication of steam-exploded lignocellulosic residues
    • Dekker F.R.H. Application of magnetic immobilized beta-glucosidase in the enzymatic saccari-fication of steam-exploded lignocellulosic residues. Appl. Biochem. Biotechnol. 23 (1990) 25
    • (1990) Appl. Biochem. Biotechnol. , vol.23 , pp. 25
    • Dekker, F.R.H.1
  • 20
  • 21
    • 0022893781 scopus 로고
    • Coupling of ligands to primary hydroxy-containing silica for high-performance affinity chromatography
    • Ernst-Cabrera K., and Wilchek M. Coupling of ligands to primary hydroxy-containing silica for high-performance affinity chromatography. Anal. Biochem. 159 (1986) 267
    • (1986) Anal. Biochem. , vol.159 , pp. 267
    • Ernst-Cabrera, K.1    Wilchek, M.2
  • 22
    • 0025826510 scopus 로고
    • Secondary metabolite biosynthesis in cultured cells of Catharanthus roseus L.G. Don immobilized by adhesion to glass fibers
    • Facchini P.J., and Dicosmo F. Secondary metabolite biosynthesis in cultured cells of Catharanthus roseus L.G. Don immobilized by adhesion to glass fibers. Appl. Microbiol. Biotechnol. 35 (1991) 382
    • (1991) Appl. Microbiol. Biotechnol. , vol.35 , pp. 382
    • Facchini, P.J.1    Dicosmo, F.2
  • 23
    • 0024593320 scopus 로고
    • Sandy alumina as substrate for economic and highly efficient immobilization of beta-glucosidase
    • Fadda M.B., Dessi M.R., Rinaldi A., and Satta G. Sandy alumina as substrate for economic and highly efficient immobilization of beta-glucosidase. Biotechnol. Bioeng. 33 (1989) 777
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 777
    • Fadda, M.B.1    Dessi, M.R.2    Rinaldi, A.3    Satta, G.4
  • 24
    • 84989104465 scopus 로고
    • Glucoamylase biosynthesis by cells of Aspergillus niger C058-III immobilized in sintered glass and pumice stones
    • Fiedurek J., and Lobarzewski J. Glucoamylase biosynthesis by cells of Aspergillus niger C058-III immobilized in sintered glass and pumice stones. Starch Staerke 42 (1990) 358
    • (1990) Starch Staerke , vol.42 , pp. 358
    • Fiedurek, J.1    Lobarzewski, J.2
  • 25
    • 84988091789 scopus 로고
    • Cellulase immobilization of iron oxide and characterization
    • Garcia III A., Oh S., and Engler C.R. Cellulase immobilization of iron oxide and characterization. Biotechnol. Bioeng. 33 (1989) 321
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 321
    • Garcia III, A.1    Oh, S.2    Engler, C.R.3
  • 26
    • 0023929184 scopus 로고
    • Characterization of a chemically modified beta-amylase immobilized on porous silica
    • Germain P., and Crichton R.R. Characterization of a chemically modified beta-amylase immobilized on porous silica. J. Chem. Technol. Biotechnol. 41 (1988) 297
    • (1988) J. Chem. Technol. Biotechnol. , vol.41 , pp. 297
    • Germain, P.1    Crichton, R.R.2
  • 27
    • 77956731437 scopus 로고
    • Natural flavor esters production by Candida Cylindracea lipase adsorbed to silica gel
    • Laane C., Trapper J., and Lilly M.D. (Eds), Elsevier Science Pub., New York
    • Gillies B., Yamazaki H., and Armstrong D.W. Natural flavor esters production by Candida Cylindracea lipase adsorbed to silica gel. In: Laane C., Trapper J., and Lilly M.D. (Eds). Biocatalysis in Organic Media, International Symposium (1987), Elsevier Science Pub., New York
    • (1987) Biocatalysis in Organic Media, International Symposium
    • Gillies, B.1    Yamazaki, H.2    Armstrong, D.W.3
  • 28
    • 0001419613 scopus 로고
    • Liquid chromatographic studies of the effect of temperature on the chiral recognition of tryptophan by silica-immobilized bovine albumin
    • Gilpin R.K., Ehtesham S.E., and Gregory R.B. Liquid chromatographic studies of the effect of temperature on the chiral recognition of tryptophan by silica-immobilized bovine albumin. Anal. Chem. 63 (1991) 2825
    • (1991) Anal. Chem. , vol.63 , pp. 2825
    • Gilpin, R.K.1    Ehtesham, S.E.2    Gregory, R.B.3
  • 29
    • 33947487769 scopus 로고
    • A water-insoluble polyanionic derivative of trypsin. 2. Effect of polyelectrolyte carrier on kinetic behavior of bound trypsin
    • Goldstein L., Levin Y., and Katchalski E. A water-insoluble polyanionic derivative of trypsin. 2. Effect of polyelectrolyte carrier on kinetic behavior of bound trypsin. Biochemistry 3 (1964) 1913
    • (1964) Biochemistry , vol.3 , pp. 1913
    • Goldstein, L.1    Levin, Y.2    Katchalski, E.3
  • 30
    • 0343619166 scopus 로고
    • Use of water-insoluble enzyme derivatives in biochemical analysis and separation
    • Goldstein L., and Katchalski E. Use of water-insoluble enzyme derivatives in biochemical analysis and separation. Fresenius Z. Anal. Chem. 243 (1968) 375
    • (1968) Fresenius Z. Anal. Chem. , vol.243 , pp. 375
    • Goldstein, L.1    Katchalski, E.2
  • 31
    • 77956719607 scopus 로고
    • Covalent immobilization of aminated silica of beta-galactosidase from Aspergillus fonseeaeus
    • Gonzalez R., Monsan P., and Ros O. Covalent immobilization of aminated silica of beta-galactosidase from Aspergillus fonseeaeus. Interferon y Biotechnol. 5 (1989) 229
    • (1989) Interferon y Biotechnol. , vol.5 , pp. 229
    • Gonzalez, R.1    Monsan, P.2    Ros, O.3
  • 32
    • 33845183900 scopus 로고
    • A new class of amperometric biosensors incorporating a polymeric electron-transfer mediator
    • Hale P.D., Inagaki T., Karan H.I., Okamoto Y., and Skotheim T.A. A new class of amperometric biosensors incorporating a polymeric electron-transfer mediator. J. Am. Chem. Soc. 1111 (1989) 3482
    • (1989) J. Am. Chem. Soc. , vol.1111 , pp. 3482
    • Hale, P.D.1    Inagaki, T.2    Karan, H.I.3    Okamoto, Y.4    Skotheim, T.A.5
  • 33
    • 0001086044 scopus 로고
    • Enzyme-immobilization by the glutaraldehyde procedure in an investigation of the effects of reducing the Schiff-bases generated as based on studying the immobilization of glucose oxidase to silanized controlled pore glass
    • Hansen E.H., and Mikkelsen H.S. Enzyme-immobilization by the glutaraldehyde procedure in an investigation of the effects of reducing the Schiff-bases generated as based on studying the immobilization of glucose oxidase to silanized controlled pore glass. Anal. Let. 24 (1991) 1419
    • (1991) Anal. Let. , vol.24 , pp. 1419
    • Hansen, E.H.1    Mikkelsen, H.S.2
  • 34
    • 0025866676 scopus 로고
    • Immobilization of fructosyl-transferring enzyme from Aweobasidium-sp on shirasu porous glass
    • Hayashi S., Ito K., Nonoguchi M., Takasaki Y., and Imada K. Immobilization of fructosyl-transferring enzyme from Aweobasidium-sp on shirasu porous glass. J. Ferment. Bioeng. 72 (1991) 68
    • (1991) J. Ferment. Bioeng. , vol.72 , pp. 68
    • Hayashi, S.1    Ito, K.2    Nonoguchi, M.3    Takasaki, Y.4    Imada, K.5
  • 35
    • 0025784916 scopus 로고
    • Continuous production of 1 kestose by beta- fructofuranosidase immobilized on shirasu porous glass
    • Hayashi S., Kinoshita J., Nonoguchi M., Takasaki Y., and Imada K. Continuous production of 1 kestose by beta- fructofuranosidase immobilized on shirasu porous glass. Biotechnol. Lett. 13 (1991) 395
    • (1991) Biotechnol. Lett. , vol.13 , pp. 395
    • Hayashi, S.1    Kinoshita, J.2    Nonoguchi, M.3    Takasaki, Y.4    Imada, K.5
  • 36
    • 0342703047 scopus 로고
    • HPLC analysis of human epidermal growth factor using immunoaffinity percolumn. I. Optimization of immunoaffinity column
    • Hayashi T., Sakamoto S., Shikanabe M., Wada I., and Yoshida H. HPLC analysis of human epidermal growth factor using immunoaffinity percolumn. I. Optimization of immunoaffinity column. Chromatographia 27 (1989) 11
    • (1989) Chromatographia , vol.27 , pp. 11
    • Hayashi, T.1    Sakamoto, S.2    Shikanabe, M.3    Wada, I.4    Yoshida, H.5
  • 37
    • 0022076706 scopus 로고
    • Fundamental studies of glucose oxidase immobilization on controlled pore glass
    • Hossain M.M., and Do D.D. Fundamental studies of glucose oxidase immobilization on controlled pore glass. Biotechnol. Bioeng. 27 (1985) 842
    • (1985) Biotechnol. Bioeng. , vol.27 , pp. 842
    • Hossain, M.M.1    Do, D.D.2
  • 38
    • 0023160706 scopus 로고
    • Extraction of thromboxane B2 from urine using an immobilized antibody column for subsequent analysis by gas chromatography-mass spectrometry
    • Hubbard H.L., Eller T.D., Mais D.E., Halushka P.V., Baker R.H., Blair I.A., Vrbanac J.J., and Daniel R. Extraction of thromboxane B2 from urine using an immobilized antibody column for subsequent analysis by gas chromatography-mass spectrometry. Prostaglandins 33 (1987) 149
    • (1987) Prostaglandins , vol.33 , pp. 149
    • Hubbard, H.L.1    Eller, T.D.2    Mais, D.E.3    Halushka, P.V.4    Baker, R.H.5    Blair, I.A.6    Vrbanac, J.J.7    Daniel, R.8
  • 39
    • 0023441577 scopus 로고
    • Isolation and purification of proteolytic enzymes on organo-silica supports with immobilized gramicidin S
    • Ignatchenko A.P., Bogomaz V.I., Tugai V.A., and Chuiko A.A. Isolation and purification of proteolytic enzymes on organo-silica supports with immobilized gramicidin S. Urk. Biokhim. Zh. 59 (1987) 28
    • (1987) Urk. Biokhim. Zh. , vol.59 , pp. 28
    • Ignatchenko, A.P.1    Bogomaz, V.I.2    Tugai, V.A.3    Chuiko, A.A.4
  • 41
    • 0025044968 scopus 로고
    • Production and stability of lignin peroxidases of Phanerochaete chrysosporium cultivated on glycerol in the presence of solid manganese-IV oxide
    • Kern H.W. Production and stability of lignin peroxidases of Phanerochaete chrysosporium cultivated on glycerol in the presence of solid manganese-IV oxide. Appl. Microbiol. Biotechnol. 33 (1990) 582
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 582
    • Kern, H.W.1
  • 43
    • 0344420753 scopus 로고
    • A simple method of cellulase immobilization on a modified silica support
    • Kitaoka M., Taniguchi H., and Sasaki T. A simple method of cellulase immobilization on a modified silica support. J. Ferment. Bioeng. 67 (1989) 182
    • (1989) J. Ferment. Bioeng. , vol.67 , pp. 182
    • Kitaoka, M.1    Taniguchi, H.2    Sasaki, T.3
  • 44
    • 0017087270 scopus 로고
    • Preparation and some properties of immobilized trypsin from the crayfish Cambarus qffinis Say
    • Kleine R., Spengenberg P., and Flemming C. Preparation and some properties of immobilized trypsin from the crayfish Cambarus qffinis Say. Hoppe-Seyler's Z. Physiol. Chem. (1976) 357
    • (1976) Hoppe-Seyler's Z. Physiol. Chem. , pp. 357
    • Kleine, R.1    Spengenberg, P.2    Flemming, C.3
  • 46
    • 0010442960 scopus 로고
    • Epoxidation of propene by microbial cells immobilized on inorganic supports
    • Kovalenko G.A., and Sokolovskii V.D. Epoxidation of propene by microbial cells immobilized on inorganic supports. Biotekhnologiya 5 (1987) 612
    • (1987) Biotekhnologiya , Issue.5 , pp. 612
    • Kovalenko, G.A.1    Sokolovskii, V.D.2
  • 47
    • 77956780220 scopus 로고
    • Double immobilization of enzymes on inorganic matrices
    • Kovalenko G.A., and Sokolovskii V.D. Double immobilization of enzymes on inorganic matrices. Biotechnol. and Bioeng. 39 (1992) 523
    • (1992) Biotechnol. and Bioeng. , vol.39 , pp. 523
    • Kovalenko, G.A.1    Sokolovskii, V.D.2
  • 49
    • 0001141301 scopus 로고
    • Immobilization of thin enzyme membranes to construct glass enzyme electrodes
    • Kumaran S., Meier H., Danna A.M., and Tran-Minh C. Immobilization of thin enzyme membranes to construct glass enzyme electrodes. Anal. Chem. 63 (1991) 1914
    • (1991) Anal. Chem. , vol.63 , pp. 1914
    • Kumaran, S.1    Meier, H.2    Danna, A.M.3    Tran-Minh, C.4
  • 50
    • 0000366910 scopus 로고
    • A high-performance liquid chromatography system with an immobilized enzyme reactor for detection of hydrophilic organic peroxides
    • Kurth H.-H., Gaeb S., Turner W.V., and Kettrup A. A high-performance liquid chromatography system with an immobilized enzyme reactor for detection of hydrophilic organic peroxides. Anal. Chem. 63 (1991) 2586
    • (1991) Anal. Chem. , vol.63 , pp. 2586
    • Kurth, H.-H.1    Gaeb, S.2    Turner, W.V.3    Kettrup, A.4
  • 52
    • 0025817777 scopus 로고
    • Single-step electroelution of proteins from SDS-polyacrylamide gels and immobilization on diisothiocyanate glass beads in prepacked capillary columns for solid-phase microsequencing
    • Liang S.-P., Lee T.T., and Laursen R.A. Single-step electroelution of proteins from SDS-polyacrylamide gels and immobilization on diisothiocyanate glass beads in prepacked capillary columns for solid-phase microsequencing. Anal. Biochem. 197 (1991) 163
    • (1991) Anal. Biochem. , vol.197 , pp. 163
    • Liang, S.-P.1    Lee, T.T.2    Laursen, R.A.3
  • 53
    • 0024962274 scopus 로고
    • Biospecific adsorption of lysozyme onto monoclonal antibody ligand immobilized on nonporous silica particles
    • Liapis A.I., Anspach B., Findley M.E., Davies J., Hearn M.T.W., and Unger K.K. Biospecific adsorption of lysozyme onto monoclonal antibody ligand immobilized on nonporous silica particles. Biotechnol. Bioeng. 34 (1989) 467
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 467
    • Liapis, A.I.1    Anspach, B.2    Findley, M.E.3    Davies, J.4    Hearn, M.T.W.5    Unger, K.K.6
  • 54
    • 77956753415 scopus 로고    scopus 로고
    • Lin, J., Chang, J., Herron, J., & Christensen, D. (1991). Immobilization of antibodies on silica surfaces for biosensor applications. Abs. Am. Chem. Soc. 20 1st Nat. Meeting, Atlanta GA, April 14--19.
    • Lin, J., Chang, J., Herron, J., & Christensen, D. (1991). Immobilization of antibodies on silica surfaces for biosensor applications. Abs. Am. Chem. Soc. 20 1st Nat. Meeting, Atlanta GA, April 14--19.
  • 55
    • 0021488346 scopus 로고
    • Production of glycolipid affinity matrices by use of heterobifunctional crosslinking agents
    • Lingwood C.A. Production of glycolipid affinity matrices by use of heterobifunctional crosslinking agents. J. Lipid Res. 25 (1984) 1010
    • (1984) J. Lipid Res. , vol.25 , pp. 1010
    • Lingwood, C.A.1
  • 57
    • 84987410592 scopus 로고
    • New matrices for the purification of pectinases by affinity chromatography
    • Lobarzewski J., Wojcik A., and Blaszczynska T. New matrices for the purification of pectinases by affinity chromatography. Acta Biotechnol. 9 (1989) 239
    • (1989) Acta Biotechnol. , vol.9 , pp. 239
    • Lobarzewski, J.1    Wojcik, A.2    Blaszczynska, T.3
  • 58
    • 0004788985 scopus 로고
    • The immobilization of animal cells in fixed and fluidized porous glass sphere reactors
    • Elsevier Science, Pub., New York
    • Looby D., Racher A.J., Griffiths J.B., and Dowsett A.B. The immobilization of animal cells in fixed and fluidized porous glass sphere reactors. Physiology of Immobilized Cells (1990), Elsevier Science, Pub., New York
    • (1990) Physiology of Immobilized Cells
    • Looby, D.1    Racher, A.J.2    Griffiths, J.B.3    Dowsett, A.B.4
  • 59
    • 0023421237 scopus 로고
    • Evaluation of the effectiveness factor along immobilized enzyme fixed-bed reactors design of a reactor with naringinase covalently immobilized into glycophase-coated porous glass
    • Manjon A., Iborra J.L., Gomez J.L., Gomez E., Bastida J., and Bodalo A. Evaluation of the effectiveness factor along immobilized enzyme fixed-bed reactors design of a reactor with naringinase covalently immobilized into glycophase-coated porous glass. Biotechnol. Bioeng. 30 (1987) 491
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 491
    • Manjon, A.1    Iborra, J.L.2    Gomez, J.L.3    Gomez, E.4    Bastida, J.5    Bodalo, A.6
  • 61
    • 0023588410 scopus 로고
    • Urease immobilization on an alkylamine derivative of titanium-IV porous silica. Kinetics and operational stability
    • Martins M.B.F., Cruz M.E.M., Cabral J.M.S., and Kennedy J.F. Urease immobilization on an alkylamine derivative of titanium-IV porous silica. Kinetics and operational stability. J. Chem. Technol. Biotechnol. 39 (1987) 201
    • (1987) J. Chem. Technol. Biotechnol. , vol.39 , pp. 201
    • Martins, M.B.F.1    Cruz, M.E.M.2    Cabral, J.M.S.3    Kennedy, J.F.4
  • 62
    • 0024416684 scopus 로고
    • Purification of argininosuccinase by high-pressure immunoaffinity chromatography on monoclonal anti-argininosuccinase-silica
    • Massom L.R., and Jarrett H.W. Purification of argininosuccinase by high-pressure immunoaffinity chromatography on monoclonal anti-argininosuccinase-silica. J. Chromatogr. 482 (1989) 252
    • (1989) J. Chromatogr. , vol.482 , pp. 252
    • Massom, L.R.1    Jarrett, H.W.2
  • 63
    • 0016167797 scopus 로고
    • Enzymes immobilized on porous ceramics
    • Messing R.A. Enzymes immobilized on porous ceramics. Biotechnol. Bioeng. 16 (1974) 1419
    • (1974) Biotechnol. Bioeng. , vol.16 , pp. 1419
    • Messing, R.A.1
  • 64
    • 0016298929 scopus 로고
    • Covalent coupling of alkaline Bacillus subtilis protease to controlled-pore silica with new simplified coupling technique
    • Messing R.A., and Stinson H.R. Covalent coupling of alkaline Bacillus subtilis protease to controlled-pore silica with new simplified coupling technique. Mol. Cell. Biochem. 4 (1974) 217-220
    • (1974) Mol. Cell. Biochem. , vol.4 , pp. 217-220
    • Messing, R.A.1    Stinson, H.R.2
  • 65
    • 77956750699 scopus 로고
    • Porous inorganic carrier materials
    • U.S. Patent No. 3, 892, 580
    • Messing, R.A. (1975). Porous inorganic carrier materials. U.S. Patent No. 3, 892, 580.
    • (1975)
    • Messing, R.A.1
  • 66
    • 84996119537 scopus 로고
    • Forced-flow bioreactor for sucrose inversion using ceramic membrane activated by silanization
    • Nakajima M., Watanabe A., Jimbo N., Nishizawa K., and Nakao S.-I. Forced-flow bioreactor for sucrose inversion using ceramic membrane activated by silanization. Biotechnol. Bioeng. 33 (1989) 856
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 856
    • Nakajima, M.1    Watanabe, A.2    Jimbo, N.3    Nishizawa, K.4    Nakao, S.-I.5
  • 67
    • 85004357715 scopus 로고
    • New enzyme reactor with forced flow of the substrate through an enzyme immobilized ceramic membrane
    • Nakajima M., Watanabe A., Nabetani H., Horikita H., and Nakoa S.-I. New enzyme reactor with forced flow of the substrate through an enzyme immobilized ceramic membrane. Agric. Biol. Chem. 52 (1988) 357
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 357
    • Nakajima, M.1    Watanabe, A.2    Nabetani, H.3    Horikita, H.4    Nakoa, S.-I.5
  • 68
    • 77956764801 scopus 로고
    • Large scale production of proteins by mammalian cells immobilized on ceramic matrix
    • Murakami H. (Ed), VCH Pub., New York
    • Niwa K., Hampson B.S., and Nicholson M.L. Large scale production of proteins by mammalian cells immobilized on ceramic matrix. In: Murakami H. (Ed). Trends in Animal Cell Culture Technology (1990), VCH Pub., New York
    • (1990) Trends in Animal Cell Culture Technology
    • Niwa, K.1    Hampson, B.S.2    Nicholson, M.L.3
  • 69
    • 0025269994 scopus 로고
    • Activity of carbonic anhydrase immobilized on porous silica beads in organic media
    • O'Daly J.P., Crumbliss A.L., and Henkens R.W. Activity of carbonic anhydrase immobilized on porous silica beads in organic media. Biotechnol. Appl. Biochem. 12 (1990) 11
    • (1990) Biotechnol. Appl. Biochem. , vol.12 , pp. 11
    • O'Daly, J.P.1    Crumbliss, A.L.2    Henkens, R.W.3
  • 71
    • 2842536697 scopus 로고
    • Isolation of bioactive lymphocyte receptors by high performance immunoaffinity chromatography
    • Phillips T.M., Faantz S.C., and Chiemlinska J.J. Isolation of bioactive lymphocyte receptors by high performance immunoaffinity chromatography. BioChromotragraphy 3 (1988) 149
    • (1988) BioChromotragraphy , vol.3 , pp. 149
    • Phillips, T.M.1    Faantz, S.C.2    Chiemlinska, J.J.3
  • 72
    • 0024110799 scopus 로고
    • Immobilization of human polymorphonuclear leukocyte myeloperoxidase onto controlled pore glass derivatives
    • Pluym B., Siegers G., and Claeys A. Immobilization of human polymorphonuclear leukocyte myeloperoxidase onto controlled pore glass derivatives. Enzyme Microb. Technol. 10 (1988) 656
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 656
    • Pluym, B.1    Siegers, G.2    Claeys, A.3
  • 75
    • 0024639479 scopus 로고
    • Physical immobilization characteristics of a hybridoma in a glass bead packed-bed reactor
    • Ramirez O.T., and Mutharasan R. Physical immobilization characteristics of a hybridoma in a glass bead packed-bed reactor. Biotechnol. Bioeng. 33 (1989) 1072
    • (1989) Biotechnol. Bioeng. , vol.33 , pp. 1072
    • Ramirez, O.T.1    Mutharasan, R.2
  • 76
    • 3342923602 scopus 로고
    • The observation of adsorpitates on a gold surface in air: Their deposition and removal using scanning tunneling microscopy
    • Roberts C., Hoffman-Millach B., and Stem W.S. The observation of adsorpitates on a gold surface in air: Their deposition and removal using scanning tunneling microscopy. Surf. Sci. 224 (1989) 1-12
    • (1989) Surf. Sci. , vol.224 , pp. 1-12
    • Roberts, C.1    Hoffman-Millach, B.2    Stem, W.S.3
  • 77
    • 0025179889 scopus 로고
    • The controlled porous glass CPG with reactive epoxy groups as support for affinity chromatography II. Modified CPG as support of substrates or coenzymes of glucose oxidase GOD for its purification and immobilization
    • Rogalski J., Dawidowicz A., Fiedurek J., and Leonowicz A. The controlled porous glass CPG with reactive epoxy groups as support for affinity chromatography II. Modified CPG as support of substrates or coenzymes of glucose oxidase GOD for its purification and immobilization. Acta Biotechnol. 10 (1990) 283
    • (1990) Acta Biotechnol. , vol.10 , pp. 283
    • Rogalski, J.1    Dawidowicz, A.2    Fiedurek, J.3    Leonowicz, A.4
  • 78
  • 80
    • 0023644458 scopus 로고
    • Immobilization of cellulolytic and hemicellulolytic enzymes on inorganic supports
    • Shimizu K., and Ishihara M. Immobilization of cellulolytic and hemicellulolytic enzymes on inorganic supports. Biotechnol. Bioeng. 29 (1987) 236
    • (1987) Biotechnol. Bioeng. , vol.29 , pp. 236
    • Shimizu, K.1    Ishihara, M.2
  • 81
    • 84985217565 scopus 로고
    • Whole cell immobilization of D-glucose isomerase enzyme on glass support
    • Shukla G.L., and Prabhu K.A. Whole cell immobilization of D-glucose isomerase enzyme on glass support. J. Basic Microbiol. 28 (1988) 457
    • (1988) J. Basic Microbiol. , vol.28 , pp. 457
    • Shukla, G.L.1    Prabhu, K.A.2
  • 82
    • 0025667796 scopus 로고
    • Selective immobilization of metalloenzymes in an acremonium---chrysogenum polyenzyme system on silica gels
    • Sokol S.V., Kiseleva L.I., Mishunin I.F., and Samodumova I.M. Selective immobilization of metalloenzymes in an acremonium---chrysogenum polyenzyme system on silica gels. Mikrobiol. Zh. (Kiev) 52 (1990) 24
    • (1990) Mikrobiol. Zh. (Kiev) , vol.52 , pp. 24
    • Sokol, S.V.1    Kiseleva, L.I.2    Mishunin, I.F.3    Samodumova, I.M.4
  • 83
    • 0024569662 scopus 로고
    • Influence of immobilization techniques on the quality of immobilized enzyme products based on porous silica carrier
    • Sorensen J.E., and Emborg C. Influence of immobilization techniques on the quality of immobilized enzyme products based on porous silica carrier. Enzyme Microb. Technol. 11 (1989) 26
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 26
    • Sorensen, J.E.1    Emborg, C.2
  • 84
    • 0026342234 scopus 로고
    • Application of a microporous glass-ceramics with a skeleton of calcium titanium phosphate to carriers for immobilization of enzymes
    • Suzuki T., Toriyama M., Hosono H., and Abe Y. Application of a microporous glass-ceramics with a skeleton of calcium titanium phosphate to carriers for immobilization of enzymes. J. Ferment. Bioeng. 5 (1991) 384
    • (1991) J. Ferment. Bioeng. , vol.5 , pp. 384
    • Suzuki, T.1    Toriyama, M.2    Hosono, H.3    Abe, Y.4
  • 86
    • 0000666271 scopus 로고
    • Direct liquid chromatographic separation of enantiomers on immobilized protein stationary phases VII. Sorbents obtained by entrapment of cross-linked bovine serum albumin in silica
    • Thompson R.A., Anderson S., and Allenmark S. Direct liquid chromatographic separation of enantiomers on immobilized protein stationary phases VII. Sorbents obtained by entrapment of cross-linked bovine serum albumin in silica. J. Chromatogr. 465 (1989) 263
    • (1989) J. Chromatogr. , vol.465 , pp. 263
    • Thompson, R.A.1    Anderson, S.2    Allenmark, S.3
  • 87
    • 33044510112 scopus 로고
    • Immobilization of potato acid phosphatase on succinamidopropyl glass beads for the dephosphorylation of bovine whole casein
    • Van Hekken D.L., Thompson M.P., and Strange E.D. Immobilization of potato acid phosphatase on succinamidopropyl glass beads for the dephosphorylation of bovine whole casein. J. Dairy Sci. 73 (1990) 2720
    • (1990) J. Dairy Sci. , vol.73 , pp. 2720
    • Van Hekken, D.L.1    Thompson, M.P.2    Strange, E.D.3
  • 88
    • 33749127816 scopus 로고
    • The structure of self-assembled monolayers of alkylsiloxanes on silicon: A comparison of results from ellipsometry and low-angle x-ray reflectivity
    • Wasserman S.R., Whitesides G.M., Tidswell I.M., Ocko B.M., Pershan P.S., and Axe J.D. The structure of self-assembled monolayers of alkylsiloxanes on silicon: A comparison of results from ellipsometry and low-angle x-ray reflectivity. J. Am. Chem. Soc. 111 (1989) 5852-5861
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5852-5861
    • Wasserman, S.R.1    Whitesides, G.M.2    Tidswell, I.M.3    Ocko, B.M.4    Pershan, P.S.5    Axe, J.D.6
  • 89
    • 0014697588 scopus 로고
    • Trypsin and papain covalently coupled to porous glass: Preparation and characterization
    • Weetall H.H. Trypsin and papain covalently coupled to porous glass: Preparation and characterization. Science 166 (1969) 615
    • (1969) Science , vol.166 , pp. 615
    • Weetall, H.H.1
  • 90
    • 0014769492 scopus 로고
    • Immobilized antigens and antibodies. Preparation and characterization
    • Weetall H.H. Immobilized antigens and antibodies. Preparation and characterization. Biochem. J. 117 (1970) 257
    • (1970) Biochem. J. , vol.117 , pp. 257
    • Weetall, H.H.1
  • 91
    • 0006654347 scopus 로고
    • Enzymes immobilized on inorganic carriers
    • Weetall H.H. Enzymes immobilized on inorganic carriers. Res. Dev. 22 (1971) 18
    • (1971) Res. Dev. , vol.22 , pp. 18
    • Weetall, H.H.1
  • 92
    • 2442493531 scopus 로고
    • Insolubilized antigens and antibodies
    • Hair M.L. (Ed), Marcel Dekker, New York
    • Weetall H.H. Insolubilized antigens and antibodies. In: Hair M.L. (Ed). Chemistry of Biosurfaces 2 (1972), Marcel Dekker, New York
    • (1972) Chemistry of Biosurfaces , vol.2
    • Weetall, H.H.1
  • 93
    • 0016077492 scopus 로고
    • Immobilized enzymes: Analytical applications
    • Weetall H.H. Immobilized enzymes: Analytical applications. Anal. Chem. 46 (1974) 602A
    • (1974) Anal. Chem. , vol.46
    • Weetall, H.H.1
  • 94
    • 0017267831 scopus 로고
    • Covalent coupling methods for inorganic supports
    • Weetall H.H. Covalent coupling methods for inorganic supports. In: Methods in Enzymology 44 (1976) 134
    • (1976) In: Methods in Enzymology , vol.44 , pp. 134
    • Weetall, H.H.1
  • 96
    • 0016227164 scopus 로고
    • Porous glass for affinity chromatography applications
    • Weetall H.H., and Filbert A.M. Porous glass for affinity chromatography applications. In: Methods in Enzymology 34 (1974) 59
    • (1974) In: Methods in Enzymology , vol.34 , pp. 59
    • Weetall, H.H.1    Filbert, A.M.2
  • 97
    • 0015988328 scopus 로고
    • Covalent binding of glucoamylase to porous glass through silane coupling. Number of covalent bonds
    • Weetall H.H., Havawala N.B., Garfinkel H.M., Buehl W.M., and Baum G. Covalent binding of glucoamylase to porous glass through silane coupling. Number of covalent bonds. Biotechnol. Bioeng. 16 (1974) 169
    • (1974) Biotechnol. Bioeng. , vol.16 , pp. 169
    • Weetall, H.H.1    Havawala, N.B.2    Garfinkel, H.M.3    Buehl, W.M.4    Baum, G.5
  • 98
    • 0016669505 scopus 로고
    • Covalent attachment of proteins to inorganic supports directly by activation with cyanogen bromide
    • Weetall H.H., and Detar C.C. Covalent attachment of proteins to inorganic supports directly by activation with cyanogen bromide. Biotechnol. Bioeng. 17 (1975) 295
    • (1975) Biotechnol. Bioeng. , vol.17 , pp. 295
    • Weetall, H.H.1    Detar, C.C.2
  • 99
    • 0024982802 scopus 로고
    • Wet chemical approaches to the characterization of organic surfaces: Self-assembled monolayers, wetting, and the physical-organic chemistry of the solid-liquid interface
    • Whitesides G.M., and Laibinis P.E. Wet chemical approaches to the characterization of organic surfaces: Self-assembled monolayers, wetting, and the physical-organic chemistry of the solid-liquid interface. Langmuir 6 (1990) 87-96
    • (1990) Langmuir , vol.6 , pp. 87-96
    • Whitesides, G.M.1    Laibinis, P.E.2
  • 100
    • 0023646129 scopus 로고
    • Silica gels activated by boron trichloride and aliphatic diamines as supports for glucoamylase immobilization
    • Wojcik A., Lobarzewski J., Blaszczynska T., and Fiedurek J. Silica gels activated by boron trichloride and aliphatic diamines as supports for glucoamylase immobilization. Biotechnol. Bioeng. 30 (1987) 983
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 983
    • Wojcik, A.1    Lobarzewski, J.2    Blaszczynska, T.3    Fiedurek, J.4
  • 101
    • 0025003122 scopus 로고
    • Immobilization of enzymes to porous-bead polymers and silica gels activated by graft polymerization of 2,3-epoxyproplymethacrylate
    • Wojcik A., Lobarzewski J., and Blaszczynska T. Immobilization of enzymes to porous-bead polymers and silica gels activated by graft polymerization of 2,3-epoxyproplymethacrylate. J. Chem. Technol. Biotechnol. 48 (1990) 287
    • (1990) J. Chem. Technol. Biotechnol. , vol.48 , pp. 287
    • Wojcik, A.1    Lobarzewski, J.2    Blaszczynska, T.3
  • 102
    • 0024278884 scopus 로고
    • Dearomatization of lignin derivatives by fungal protocatechuate 3,4-dioxygenase immobilized on porosity glass
    • Wojtas-Wasilewska M., Luterek J., Leonowicz A., and Dawidowicz A. Dearomatization of lignin derivatives by fungal protocatechuate 3,4-dioxygenase immobilized on porosity glass. Biotechnol. Bioeng. 32 (1988) 507
    • (1988) Biotechnol. Bioeng. , vol.32 , pp. 507
    • Wojtas-Wasilewska, M.1    Luterek, J.2    Leonowicz, A.3    Dawidowicz, A.4


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